Academic journal article Alcohol Research

Proteomics in Alcohol Research

Academic journal article Alcohol Research

Proteomics in Alcohol Research

Article excerpt

Researchers are interested not only in the genes that may contribute to the development of alcoholism but also in the functions and activities of the proteins encoded by those genes. The relatively new field of proteomics--the large-scale analysis of protein structure and function as well as of protein--protein interactions--may allow substantial progress in this endeavor. Drs. Helen Anni and Yedy Israel present some of the techniques used in proteomics analyses, such as two-dimensional gel electrophoresis, high-performance liquid chromatography, and their modifications, as well as potential applications of these technologies in the alcohol field. Together with other sophisticated techniques for studying protein--protein interactions, these approaches eventually will provide valuable information on the mechanisms underlying the development of alcoholism and alcohol-induced organ damage. (pp. 219-232)

The proteome is the complete set of proteins in an organism. It is considerably larger and more complex than the genome--the collection of genes that encodes these proteins. Proteomics deals with the qualitative and quantitative study of the proteome under physiological and pathological conditions (e.g., after exposure to alcohol, which causes major changes in numerous proteins of different cell types). To map large proteomes such as the human proteome, proteins from discrete tissues, cells, cell components, or biological fluids are first separated by high-resolution two-dimensional electrophoresis and multidimensional liquid chromatography. Then, individual proteins are identified by mass spectrometry. The huge amount of data acquired using these techniques is analyzed and assembled by fast computers and bioinformatics tools. Using these methods, as well as other technological advances, alcohol researchers can gain a better understanding of how alcohol globally influences protein structure and function, protein-protein interactions, and protein networks. This knowledge ultimately will assist in the early diagnosis and prognosis of alcoholism and the discovery of new drug targets and medications for treatment. KEY WORDS: proteins; protein metabolism; physiological AODE (alcohol and other drug effects); alcoholic beverage; genetic mapping; gene expression; AODR (alcohol and other drug related) biological markers; signal transduction; field separation method; research agenda


The proteome is defined as the collection of all the proteins in an organism. The human proteome has been estimated to have over 1 million proteins, which are found in the approximately 250 different cell types under various physiological and pathological conditions. Compared with the genome--the entire set of genes that encode the proteins--the proteome is much larger and more complex. Several reasons contribute to the greater size and complexity of the proteome:

* The genetic information contained in some genes can be converted into more than one protein per gene through a process called differential splicing.

* A plethora of changes in protein structure, called post-translational modifications (PTMs), can occur after protein synthesis.

* Many proteins do not act alone but interact with other proteins to transmit biological signals and regulate cell function.

Thus, unlike the genome, which consists of a fixed number of genes that are turned on or off, the proteome is a more dynamic system. External stimuli, such as exposure to alcohol, also can affect numerous proteins in terms of their abundance, and the types of PTMs they undergo. In addition, alcohol exposure may shift the types of proteins that are produced in a cell--for example, favoring regulatory proteins that add phosphate groups to other proteins (i.e., kinases) to modulate protein activity over proteins that remove those phosphate groups (i.e., phosphatases).

The term "proteomics" refers to the large-scale analysis of protein structure, function, and interactions. …

Search by... Author
Show... All Results Primary Sources Peer-reviewed


An unknown error has occurred. Please click the button below to reload the page. If the problem persists, please try again in a little while.